Cited by 345Cellular transport and secretionGlycosylation and Glycoproteins ResearchAutophagy in Disease and Therapy

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Isolation and characterization of human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Major sialoglycoproteins carrying polylactosaminoglycan.

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Carlsson, S R, Roth, J, Piller, F, Fukuda, M·1988·Journal of Biological Chemistry

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Abstract

Two major lysosomal membrane glycoproteins with apparent Mr approximately 120,000 were purified from chronic myelogenous leukemia cells. These glycoproteins are major sialoglycoproteins containing polylactosaminoglycan and represent approximately 0.1-0.2% of total cell proteins. A monoclonal antibody specific to one of the glycoproteins and polyclonal antibodies specific to the other glycoprotein were obtained. Immunoelectron microscopic examination of HeLa cells revealed that these two glycoproteins mainly reside in lysosomes and multivesicular bodies. Immunoprecipitation experiments showed that a number of different cell lines express these glycoproteins. However, the apparent molecular weights differed between cell lines; this probably represents differences in the amount of polylactosaminoglycan expressed by each cell line. As shown in the following paper (Fukuda, M., Viitala, J., Matteson, J., and Carlsson, S. R. (1988) J. Biol. Chem. 263, 18920-18928) one of the glycoproteins is very homologous to that of a mouse counterpart, m-lamp-1. The human form of this glycoprotein is therefore named human lamp-1 (h-lamp-1), while the other glycoprotein, to which the monoclonal antibody was made, is called human lamp-2 (h-lamp-2). Pulse-chase labeling experiments detected that h-lamp-1 and h-lamp-2 are produced first as precursor forms of 87.5 and 84 kDa, and treatment with endo-beta-N-acetylglucosaminidase H (endo-H) or endo-beta-N-acetylglucosaminidase F (endo-F) reduced their m…

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Authors: Carlsson, S. R., Roth, J., Piller, F., & Fukuda, M.
Affiliations: Sanford Burnham Prebys Medical Discovery Institute (US)
ORCID: Carlsson, S R
Fukuda, M
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1988-12
Volume: 263
Issue: 35
Pages: 18911-18919
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(18)37369-1
OpenAlex: W1525792717
Cited by: 345
References: 55
Citations by year: 2026: 5 · 2025: 4 · 2024: 4 · 2023: 7 · 2022: 6 · 2021: 5 · 2020: 7 · 2019: 4 · 2018: 2 · 2017: 4 · 2016: 6 · 2015: 6 · 2014: 8 · 2013: 7 · 2012: 10
FWCI: 4.22
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 11641 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Cancer Institute (CA 28896)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Keywords: lysosomal membrane glycoprotein, LAMP1, LAMP2, lysosomes, multivesicular bodies, sialoglycoproteins, N-glycosylation, sialic acid, monoclonal antibodies, endo-beta-N-acetylglucosaminidase H, HeLa cells
MeSH terms: Amino Acids, Amino Sugars, Antibodies, Monoclonal, Carbohydrates, Cell Line, Glycoside Hydrolases, Humans, Lysosomes, Membrane Glycoproteins, Molecular Weight, Polymers, Polysaccharides, Sialoglycoproteins, Leukemia, Myeloid, Acute, Antigens, CD, Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase, Lysosomal Membrane Proteins

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Isolation and characterization of human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Major sialoglycoproteins carrying polylactosaminoglycan.

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